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• W2101825447 abstract "Although their amino acid sequences and structure closely resemble DNA methyltransferases, Dnmt2 proteins were recently shown by Goll and colleagues to function as RNA methyltransferases transferring a methyl group to the C5 position of C38 in tRNA Asp . We observe that human DNMT2 methylates tRNA isolated from Dnmt2 knock-out Drosophila melanogaster and Dictyostelium discoideum . RNA extracted from wild type D. melanogaster was methylated to a lower degree, but in the case of Dictyostelium , there was no difference in the methylation of RNA isolated from wild-type and Dnmt2 knock-out strains. Methylation of in vitro transcribed tRNA Asp confirms it to be a target of DNMT2. Using site directed mutagenesis, we show here that the enzyme has a DNA methyltransferase-like mechanism, because similar residues from motifs IV, VI, and VIII are involved in catalysis as identified in DNA methyltransferases. In addition, exchange of C292, which is located in a CFT motif conserved among Dnmt2 proteins, strongly reduced the catalytic activity of DNMT2. Dnmt2 represents the first example of an RNA methyltransferase using a DNA methyltransferase type of mechanism." @default.
• W2101825447 created "2016-06-24" @default.
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• W2101825447 date "2008-06-20" @default.
• W2101825447 modified "2023-10-01" @default.
• W2101825447 title "Human DNMT2 methylates tRNA^Asp molecules using a DNA methyltransferase-like catalytic mechanism" @default.
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• W2101825447 doi "https://doi.org/10.1261/rna.970408" @default.
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